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Spectroscopic Characterization of Intermolecular Interaction of Amyloid β Promoted on GM1 Micelles
- Source :
- International Journal of Alzheimer's Disease, Vol 2011 (2011)
- Publication Year :
- 2011
- Publisher :
- Wiley, 2011.
-
Abstract
- Clusters of GM1 gangliosides act as platforms for conformational transition of monomeric, unstructured amyloid β (Aβ) to its toxic β-structured aggregates. We have previously shown that Aβ(1–40) accommodated on the hydrophobic/hydrophilic interface of lyso-GM1 or GM1 micelles assumes α-helical structures under ganglioside-excess conditions. For better understanding of the mechanisms underlying the α-to-β conformational transition of Aβ on GM1 clusters, we performed spectroscopic characterization of Aβ(1–40) titrated with GM1. It was revealed that the thioflavin T- (ThT-) reactive β-structure is more populated in Aβ(1–40) under conditions where the Aβ(1–40) density on GM1 micelles is high. Under this circumstance, the C-terminal hydrophobic anchor Val39-Val40 shows two distinct conformational states that are reactive with ThT, while such Aβ species were not generated by smaller lyso-GM1 micelles. These findings suggest that GM1 clusters promote specific Aβ-Aβ interactions through their C-termini coupled with formation of the ThT-reactive β-structure depending on sizes and curvatures of the clusters.
Details
- Language :
- English
- ISSN :
- 20900252
- Volume :
- 2011
- Database :
- Directory of Open Access Journals
- Journal :
- International Journal of Alzheimer's Disease
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.0f2e7529eb5f40b28c05c9c7923f7398
- Document Type :
- article
- Full Text :
- https://doi.org/10.4061/2011/925073